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Spectroscopic and electronic structu...

Skulan, Andrew John.

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Spectroscopic and electronic structure investigations of the oxygen-activating intermediates of ribonucleotide reductase.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Spectroscopic and electronic structure investigations of the oxygen-activating intermediates of ribonucleotide reductase./
Author:	Skulan, Andrew John.
Description:	209 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5498.
Contained By:	Dissertation Abstracts International64-11B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3111793
ISBN:	0496593234

Spectroscopic and electronic structure investigations of the oxygen-activating intermediates of ribonucleotide reductase.
Skulan, Andrew John.

Spectroscopic and electronic structure investigations of the oxygen-activating intermediates of ribonucleotide reductase. - 209 p.

Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5498.

Thesis (Ph.D.)--Stanford University, 2004.

Circular dichroism (CD) and magnetic circular dichroism (MCD) data, combined with spin-Hamiltonian analysis and correlated with density functional theory (DFT) calculations allow identification of the active site geometries for biferrous wt- and W48F/D84E-R2 subunit of ribonucleotide reductase. This study probes the effect of varying the ligand set, the positions of coordinated water molecules and additional protein constraints on the geometry and energy of the binuclear site.

ISBN: 0496593234Subjects--Topical Terms:

586156
Chemistry, Analytical.

Spectroscopic and electronic structure investigations of the oxygen-activating intermediates of ribonucleotide reductase.
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020 $a 0496593234
035 $a (UnM)AAI3111793
035 $a AAI3111793
040 $a UnM $c UnM
100 1 $a Skulan, Andrew John. $3 1932308
245 1 0 $a Spectroscopic and electronic structure investigations of the oxygen-activating intermediates of ribonucleotide reductase.
300 $a 209 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5498.
500 $a Adviser: Edward I. Solomon.
502 $a Thesis (Ph.D.)--Stanford University, 2004.
520 $a Circular dichroism (CD) and magnetic circular dichroism (MCD) data, combined with spin-Hamiltonian analysis and correlated with density functional theory (DFT) calculations allow identification of the active site geometries for biferrous wt- and W48F/D84E-R2 subunit of ribonucleotide reductase. This study probes the effect of varying the ligand set, the positions of coordinated water molecules and additional protein constraints on the geometry and energy of the binuclear site.
520 $a The geometric and electronic structure of the peroxo intermediate of the W48F/D84E-R2 variant was studied and related to the putative kinetically masked peroxo intermediate of wt-R2. The spectroscopic signatures of the W48F/D84E-R2 peroxo intermediate were found to be consistent only with the cis -mu-1,2 peroxo coordination geometry. DFT geometry optimizations using a model including the constraints imposed by the wt- and W48F/D84E-R2 active site ligand sets identifies cis-mu-1,2 peroxo as the most stable intermediate structure. This study produces new insight into the electronic structure of the experimentally defined peroxo intermediate, structurally similar model complexes and other biological biferric peroxo intermediates.
520 $a The high-valent intermediates of oxygen activation are poorly characterized and their structures are still a matter of debate. To investigate the nature of the high-valent bis-mu-oxo core, the spectroscopic properties and electronic structure of the structurally defined Fe2(III,IV) complex, [Fe 2O2(5-Et3-TPA)2](ClO4) 3 where 5-Et3-TPA=tris(5-ethyl-2-pyridylmethyl)amine were explored. Analysis of absorption, MCD, resonance Raman profiles and VTVH MCD saturation behavior allows transition assignments and calibration of density functional calculations. The C2h geometric distortion of the Fe 2O2 core is due to asymmetry in the capping ligand and results in a small (&sim;20%) difference in bond strength between adjacent Fe--O bonds. Density functional calculations also identify the orbital origins of the unique magnetic features of this core and identify the three singly-occupied pi* metal-based orbitals that form strong superexchange pathways which lead to valence delocalization and the S = 32 ground state. Frontier molecular orbital (FMO) theory identifies these orbitals as key to the observed reactivity of this complex as they overlap with the substrate C--H bonding orbital in the best trajectory for hydrogen atom abstraction. The electronic structure implications of these results for the high-valent enzyme intermediates are discussed.
590 $a School code: 0212.
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0486
710 2 0 $a Stanford University. $3 754827
773 0 $t Dissertation Abstracts International $g 64-11B.
790 1 0 $a Solomon, Edward I., $e advisor
790 $a 0212
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3111793